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- W2078347406 abstract "Pathogen-induced remodelling of the host cell actin cytoskeleton drives internalization of invasive Salmonella by non-phagocytic intestinal epithelial cells. Two Salmonella actin-binding proteins are involved in internalization: SipC is essential for the process, while SipA enhances its efficiency. Using purified SipC and SipA proteins in in vitro assays of actin dynamics and F-actin bundling, we demonstrate that SipA stimulates substantially SipC-mediated nucleation of actin polymerization. SipA additionally enhances SipC-mediated F-actin bundling, and SipC-SipA collaboration generates stable networks of F-actin bundles. The data show that bacterial SipC and SipA cooperate to direct efficient modulation of actin dynamics, independently of host cell proteins. The ability of SipA to enhance SipC-induced reorganization of the actin cytoskeleton in vivo was confirmed using semi-permeabilized cultured mammalian cells." @default.
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- W2078347406 date "2001-05-01" @default.
- W2078347406 modified "2023-10-18" @default.
- W2078347406 title "Cooperation between actin-binding proteins of invasive Salmonella: SipA potentiates SipC nucleation and bundling of actin" @default.
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- W2078347406 doi "https://doi.org/10.1093/emboj/20.9.2131" @default.
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